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Cryo-EM structure of the bacterial actin AlfA reveals unique assembly and ATP-binding interactions and the absence of a conserved subdomain
Gulsima Usluer, Frank Dimaio, Shunkai Yang, Jesse M. Hansen, Jessica K. Polka, R. Dyche Mullins, Justin M. Kollman
doi: https://doi.org/10.1101/186080
Gulsima Usluer
aDepartment of Biochemistry, University of Washington, Seattle, WA 98103
Frank Dimaio
aDepartment of Biochemistry, University of Washington, Seattle, WA 98103
Shunkai Yang
bDepartment of Anatomy & Cell Biology, McGill University, Montreal, QC H3A 0C7
Jesse M. Hansen
aDepartment of Biochemistry, University of Washington, Seattle, WA 98103
Jessica K. Polka
cDepartment of Cellular and Molecular Pharmacology, University of California San Francisico, CA 94158
R. Dyche Mullins
cDepartment of Cellular and Molecular Pharmacology, University of California San Francisico, CA 94158
Justin M. Kollman
aDepartment of Biochemistry, University of Washington, Seattle, WA 98103
Article usage
Posted September 07, 2017.
Cryo-EM structure of the bacterial actin AlfA reveals unique assembly and ATP-binding interactions and the absence of a conserved subdomain
Gulsima Usluer, Frank Dimaio, Shunkai Yang, Jesse M. Hansen, Jessica K. Polka, R. Dyche Mullins, Justin M. Kollman
bioRxiv 186080; doi: https://doi.org/10.1101/186080
Cryo-EM structure of the bacterial actin AlfA reveals unique assembly and ATP-binding interactions and the absence of a conserved subdomain
Gulsima Usluer, Frank Dimaio, Shunkai Yang, Jesse M. Hansen, Jessica K. Polka, R. Dyche Mullins, Justin M. Kollman
bioRxiv 186080; doi: https://doi.org/10.1101/186080
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